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Transmembrane Emp24-Like Trafficking Protein 10 (Yeast) (TMED10) (Center) antibody

Details for Product No. ABIN500992, Supplier: Log in to see
Antigen
  • tmp21
  • P24(DELTA)
  • S31I125
  • S31III125
  • TMP21
  • Tmp-21-I
  • p23
  • 1110014C03Rik
  • Tmp21
  • p24delta1
  • fe06g04
  • wu:fb98e10
  • wu:fe06g04
  • zgc:85681
Epitope
Center
40
13
10
4
2
2
1
1
1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
84
43
43
4
2
1
1
1
1
1
1
1
Host
Rabbit
71
14
2
Clonality
Polyclonal
Conjugate
Un-conjugated
4
3
3
3
3
3
1
1
1
1
1
1
1
1
1
Application
Enzyme Immunoassay (EIA), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
63
42
26
13
11
4
1
Supplier
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Immunogen TMP21 antibody was raised against a 18 amino acid peptide from near the center of human TMP21.
Isotype IgG
Specificity This antibody detects TMED10 / TMP21 at Center.
Cross-Reactivity (Details) Species reactivity (tested):Human, mouse, rat
Purification Peptide affinity chromatography
Alternative Name TMED10 / TMP21 (TMED10 Antibody Abstract)
Background TMP21 is a ubiquitously expressed protein that is involved in vesicular targeting and protein transport. More recent experiments have shown that it is also a component in the presenilin complex and modulates the γ-secretase but not theεsecretase cleavage activity of the amyloid precursor protein. The presenilin complex is composed of the proteins APH1, nicastrin, and PEN2 in addition to presenilin-1. Together, these proteins cleave the amyloid precursor protein at what is known as the γ and ε-sites and can lead to the accumulation of the Aβ cleavage product that is associated with Alzheimer's disease. Co-immunoprecipitation experiments using antibodies against these proteins also yielded TMP21 indicating that TMP21 may play a role in the regulation of this complex. Suppression of TMP21 expression by siRNA in transfected cells caused increased γ-secretase activity but not ε-secretase activity, and increased Aβ production, demonstrating that TMP21 can modulate γsecretase activity.Synonyms: 21 kDa transmembrane-trafficking protein, S31I125, Transmembrane emp24 domain-containing protein 10, Transmembrane protein Tmp21
Gene ID 10972
Application Notes ELISA. Western blot: 1 - 2 μg/mL. Immunohistochemistry on paraffin sections.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Buffer PBS containing 0.02 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store at 2 - 8 °C for up to one month or (in aliquots) at -20 °C for longer.
Supplier Images
Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)) image for anti-Transmembrane Emp24-Like Trafficking Protein 10 (Yeast) (TMED10) (Center) antibody (ABIN500992) Immunohistochemistry of TMP21 in human brain tissue with this product at 5 μg/ml.
Western Blotting (WB) image for anti-Transmembrane Emp24-Like Trafficking Protein 10 (Yeast) (TMED10) (Center) antibody (ABIN500992) Western blot analysis of TMP21 in mouse brain tissue lysate with this product at (A) ...
Background publications Chen, Hasegawa, Schmitt-Ulms et al.: "TMP21 is a presenilin complex component that modulates gamma-secretase but not epsilon-secretase activity." in: Nature, Vol. 440, Issue 7088, pp. 1208-12, 2006 (PubMed).

Periz, Fortini: "Functional reconstitution of gamma-secretase through coordinated expression of presenilin, nicastrin, Aph-1, and Pen-2." in: Journal of neuroscience research, Vol. 77, Issue 3, pp. 309-22, 2004 (PubMed).

Selkoe: "The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease." in: Trends in cell biology, Vol. 8, Issue 11, pp. 447-53, 1999 (PubMed).

Blum, Feick, Puype et al.: "Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular trafficking." in: The Journal of biological chemistry, Vol. 271, Issue 29, pp. 17183-9, 1996 (PubMed).